共 48 条
Enantioselective reductions of ethyl 2-oxo-4-phenylbutyrate by Saccharomyces cerevisiae dehydrogenases
被引:46
作者:

Kaluzna, I
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机构: Univ Florida, Dept Chem, Gainesville, FL 32611 USA

Andrew, AA
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机构: Univ Florida, Dept Chem, Gainesville, FL 32611 USA

Bonilla, M
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机构: Univ Florida, Dept Chem, Gainesville, FL 32611 USA

Martzen, MR
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机构: Univ Florida, Dept Chem, Gainesville, FL 32611 USA

Stewart, JD
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机构:
Univ Florida, Dept Chem, Gainesville, FL 32611 USA Univ Florida, Dept Chem, Gainesville, FL 32611 USA
机构:
[1] Univ Florida, Dept Chem, Gainesville, FL 32611 USA
[2] Ceptyr, Bothell, WA 98021 USA
基金:
美国国家科学基金会;
关键词:
glutathione;
baker's yeast;
angiotensin converting enzyme;
D O I:
10.1016/S1381-1177(02)00006-1
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
A set of fusion proteins consisting of glutathione S-transferase linked to the N-terminus of putative dehydrogenases produced by baker's yeast (Saccharomyces cerevisiae) was screened for the reduction of ethyl 2-oxo-4-phenylbutyrate in the presence of NADH and NADPH. Two dehydrogenases-Ypr1p and Gre2p-rapidly reduced this alpha-ketoester, providing the (R)and (S)-alcohol, respectively, with high stereoselectivities. The same enzymes were over-expressed in their native forms in Escherichia coli and growing cells of the engineered strains could also be used to carry out the reductions without the need for exogenous cofactor. These results demonstrate the power of genomic fusion protein libraries to identify appropriate biocatalysts rapidly and expedite process development. (C) 2002 Elsevier Science B.V. All rights reserved.
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页码:101 / 105
页数:5
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